TEAD1

TEA domain family member 1 (SV40 transcriptional enhancer factor)

PDB rendering based on 2hzd.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2HZD, 3KYS, 4RE1

Identifiers

Symbols

TEAD1 ; AA; NTEF-1; REF1; TCF-13; TCF13; TEAD-1; TEF-1

External IDs

OMIM: 189967 MGI: 101876 HomoloGene: 2418 GeneCards: TEAD1 Gene

Gene ontology
Molecular function	• DNA binding • transcription factor activity, sequence-specific DNA binding • protein binding
Cellular component	• nucleoplasm • cytoplasm • Golgi apparatus
Biological process	• regulation of transcription, DNA-templated • transcription initiation from RNA polymerase II promoter • gene expression • hippo signaling
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
12.67 – 12.94 Mb

Chr 7:
112.68 – 112.91 Mb

PubMed search

Transcriptional enhancer factor TEF-1 is a protein that in humans is encoded by the TEAD1 gene.^[1]^[2]^[3]^[4]

Function

TEAD1 is a member of the mammalian TEAD transcription factor family (initially named the transcriptional enhancer factor (TEF) family), which contain the TEA/ATTS DNA-binding domain.^[5]

Interactions

TEAD1 has been shown to interact with MEF2C,^[6] Serum response factor^[7] and MAX.^[8]

References

↑ Xiao JH, Davidson I, Matthes H, Garnier JM, Chambon P (May 1991). "Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1". Cell 65 (4): 551–68. doi:10.1016/0092-8674(91)90088-G. PMID 1851669.
↑ Jacquemin P, Depetris D, Mattei MG, Martial JA, Davidson I (Jan 1999). "Localization of human transcription factor TEF-4 and TEF-5 (TEAD2, TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence in situ hybridization and radiation hybrid analysis". Genomics 55 (1): 127–9. doi:10.1006/geno.1998.5628. PMID 9889009.
↑ Fossdal R, Jonasson F, Kristjansdottir GT, Kong A, Stefansson H, Gosh S, Gulcher JR, Stefansson K (May 2004). "A novel TEAD1 mutation is the causative allele in Sveinsson's chorioretinal atrophy (helicoid peripapillary chorioretinal degeneration)". Human Molecular Genetics 13 (9): 975–81. doi:10.1093/hmg/ddh106. PMID 15016762.
↑ "Entrez Gene: TEAD1 TEA domain family member 1 (SV40 transcriptional enhancer factor)".
↑ Bürglin TR (Jul 1991). "The TEA domain: a novel, highly conserved DNA-binding motif". Cell 66 (1): 11–2. doi:10.1016/0092-8674(91)90132-I. PMID 2070413.
↑ Maeda T, Gupta MP, Stewart AF (Jun 2002). "TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters". Biochemical and Biophysical Research Communications 294 (4): 791–7. doi:10.1016/S0006-291X(02)00556-9. PMID 12061776.
↑ Gupta M, Kogut P, Davis FJ, Belaguli NS, Schwartz RJ, Gupta MP (Mar 2001). "Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1". The Journal of Biological Chemistry 276 (13): 10413–22. doi:10.1074/jbc.M008625200. PMID 11136726.
↑ Gupta MP, Amin CS, Gupta M, Hay N, Zak R (Jul 1997). "Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression". Molecular and Cellular Biology 17 (7): 3924–36. doi:10.1128/mcb.17.7.3924. PMC 232245. PMID 9199327.

Boam DS, Davidson I, Chambon P (Aug 1995). "A TATA-less promoter containing binding sites for ubiquitous transcription factors mediates cell type-specific regulation of the gene for transcription enhancer factor-1 (TEF-1)". The Journal of Biological Chemistry 270 (33): 19487–94. doi:10.1074/jbc.270.33.19487. PMID 7642633.
Fossdal R, Magnússon L, Weber JL, Jensson O (Mar 1995). "Mapping the locus of atrophia areata, a helicoid peripapillary chorioretinal degeneration with autosomal dominant inheritance, to chromosome 11p15". Human Molecular Genetics 4 (3): 479–83. doi:10.1093/hmg/4.3.479. PMID 7795606.
Kariya K, Farrance IK, Simpson PC (Dec 1993). "Transcriptional enhancer factor-1 in cardiac myocytes interacts with an alpha 1-adrenergic- and beta-protein kinase C-inducible element in the rat beta-myosin heavy chain promoter". The Journal of Biological Chemistry 268 (35): 26658–62. PMID 8253797.
Shimizu N, Smith G, Izumo S (Aug 1993). "Both a ubiquitous factor mTEF-1 and a distinct muscle-specific factor bind to the M-CAT motif of the myosin heavy chain beta gene". Nucleic Acids Research 21 (17): 4103–10. doi:10.1093/nar/21.17.4103. PMC 310013. PMID 8396764.
Stewart AF, Richard CW, Suzow J, Stephan D, Weremowicz S, Morton CC, Adra CN (Oct 1996). "Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene preferentially expressed in skeletal muscle: evidence for an ancient multigene family". Genomics 37 (1): 68–76. doi:10.1006/geno.1996.0522. PMID 8921372.
Gupta MP, Amin CS, Gupta M, Hay N, Zak R (Jul 1997). "Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression". Molecular and Cellular Biology 17 (7): 3924–36. doi:10.1128/mcb.17.7.3924. PMC 232245. PMID 9199327.
Simmonds AJ, Liu X, Soanes KH, Krause HM, Irvine KD, Bell JB (Dec 1998). "Molecular interactions between Vestigial and Scalloped promote wing formation in Drosophila". Genes & Development 12 (24): 3815–20. doi:10.1101/gad.12.24.3815. PMC 317270. PMID 9869635.
Vaudin P, Delanoue R, Davidson I, Silber J, Zider A (Nov 1999). "TONDU (TDU), a novel human protein related to the product of vestigial (vg) gene of Drosophila melanogaster interacts with vertebrate TEF factors and substitutes for Vg function in wing formation". Development 126 (21): 4807–16. PMID 10518497.
Gupta M, Kogut P, Davis FJ, Belaguli NS, Schwartz RJ, Gupta MP (Mar 2001). "Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1". The Journal of Biological Chemistry 276 (13): 10413–22. doi:10.1074/jbc.M008625200. PMID 11136726.
Vassilev A, Kaneko KJ, Shu H, Zhao Y, DePamphilis ML (May 2001). "TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm". Genes & Development 15 (10): 1229–41. doi:10.1101/gad.888601. PMC 313800. PMID 11358867.
Carlini LE, Getz MJ, Strauch AR, Kelm RJ (Mar 2002). "Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle cells. Suppression of TEF-1 mediated activation by the single-stranded DNA-binding proteins, Pur alpha, Pur beta, and MSY1". The Journal of Biological Chemistry 277 (10): 8682–92. doi:10.1074/jbc.M109754200. PMID 11751932.
Maeda T, Gupta MP, Stewart AF (Jun 2002). "TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters". Biochemical and Biophysical Research Communications 294 (4): 791–7. doi:10.1016/S0006-291X(02)00556-9. PMID 12061776.
Maeda T, Chapman DL, Stewart AF (Dec 2002). "Mammalian vestigial-like 2, a cofactor of TEF-1 and MEF2 transcription factors that promotes skeletal muscle differentiation". The Journal of Biological Chemistry 277 (50): 48889–98. doi:10.1074/jbc.M206858200. PMID 12376544.
Thompson M, Andrade VA, Andrade SJ, Pusl T, Ortega JM, Goes AM, Leite MF (Feb 2003). "Inhibition of the TEF/TEAD transcription factor activity by nuclear calcium and distinct kinase pathways". Biochemical and Biophysical Research Communications 301 (2): 267–74. doi:10.1016/S0006-291X(02)03024-3. PMID 12565854.
Karasseva N, Tsika G, Ji J, Zhang A, Mao X, Tsika R (Aug 2003). "Transcription enhancer factor 1 binds multiple muscle MEF2 and A/T-rich elements during fast-to-slow skeletal muscle fiber type transitions". Molecular and Cellular Biology 23 (15): 5143–64. doi:10.1128/MCB.23.15.5143-5164.2003. PMC 165722. PMID 12861002.
Günther S, Mielcarek M, Krüger M, Braun T (2004). "VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation". Nucleic Acids Research 32 (2): 791–802. doi:10.1093/nar/gkh248. PMC 373362. PMID 14762206.

PDB gallery

2hzd: NMR structure of the DNA-binding TEA domain and insights into TEF-1 function

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor AATF 1 2 3 4 5 6 7 AP-1 c-Fos FOSB FOSL1 FOSL2 JDP2 c-Jun JUNB JunD BACH 1 2 BATF BLZF1 C/EBP α β γ δ ε ζ CREB 1 3 L1 CREM DBP DDIT3 GABPA HLF MAF B F G K NFE 2 L1 L2 L3 NFIL3 NRL NRF 1 2 3 XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 AhR AHRR ARNT ASCL1 BHLH 2 3 9 ARNTL ARNTL ARNTL2 CLOCK EPAS1 FIGLA HAND 1 2 HES 5 6 HEY 1 2 L HES1 HIF 1A 3A ID 1 2 3 4 LYL1 MESP2 MXD4 MYCL1 MYCN Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 Neurogenins 1 2 3 NeuroD 1 2 NPAS 1 2 3 OLIG 1 2 Pho4 Scleraxis SIM 1 2 TAL 1 2 Twist USF1

(1.3) bHLH-ZIP	AP-4 MAX MXD3 MITF MNT MLX MXI1 Myc SREBP 1 2

(1.4) NF-1	NFI A B C X SMAD R-SMAD 1 2 3 5 9 I-SMAD 6 7 4)

(1.5) RF-X	RFX 1 2 3 4 5 6 ANK

(1.6) Basic helix-span-helix (bHSH)	AP-2 α β γ δ ε

(2) Zinc finger DNA-binding domains

(2.1) Nuclear receptor (Cys₄)

subfamily 1	Thyroid hormone α β CAR FXR LXR α β PPAR α β/δ γ PXR RAR α β γ ROR α β γ Rev-ErbA α β VDR

subfamily 2	COUP-TF (I II Ear-2 HNF4 α γ PNR RXR α β γ Testicular receptor 2 4 TLX

subfamily 3	Steroid hormone Androgen Estrogen α β Glucocorticoid Mineralocorticoid Progesterone Estrogen related α β γ

subfamily 4	NUR NGFIB NOR1 NURR1

subfamily 5	LRH-1 SF1

subfamily 6	GCNF

subfamily 0	DAX1 SHP

(2.2) Other Cys₄

GATA
- 1
- 2
- 3
- 4
- 5
- 6
MTA
- 1
- 2
- 3
TRPS1

(2.3) Cys₂His₂

General transcription factors
- TFIIA
- TFIIB
- TFIID
- TFIIE
  - 1
  - 2
- TFIIF
- 1
- 2
  - TFIIH
  - 1
  - 2
  - 4
  - 2I
  - 3A
  - 3C1
  - 3C2

ATBF1
BCL
- 6
- 11A
- 11B
CTCF
E4F1
EGR
- 1
- 2
- 3
- 4
ERV3
GFI1
GLI-Krüppel family
- 1
- 2
- 3
- REST
- S1
- S2
- YY1
HIC
- 1
- 2
HIVEP
- 1
- 2
- 3
IKZF
- 1
- 2
- 3
ILF
- 2
- 3
KLF
- 1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15
- 17
MTF1
MYT1
OSR1
PRDM9
SALL
- 1
- 2
- 3
- 4
SP
- 1
- 2
- 4
- 7
- 8
TSHZ3
WT1
Zbtb7
- 7A
- 7B
ZBTB
- 11
- 16
- 17
- 20
- 32
- 33
- 40
zinc finger
- 3
- 7
- 9
- 10
- 19
- 22
- 24
- 33B
- 34
- 35
- 41
- 43
- 44
- 51
- 74
- 143
- 146
- 148
- 165
- 202
- 217
- 219
- 238
- 239
- 259
- 267
- 268
- 281
- 295
- 300
- 318
- 330
- 346
- 350
- 365
- 366
- 384
- 423
- 451
- 452
- 471
- 593
- 638
- 644
- 649
- 655

(2.4) Cys₆

HIVEP1

(2.5) Alternating composition

AIRE
DIDO1
GRLF1
ING
- 1
- 2
- 4
JARID
- 1A
- 1B
- 1C
- 1D
- 2
JMJD1B

(2.6) WRKY

WRKY

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX CDX 1 2 CRX CUTL1 DBX 1 2 DLX 3 4 5 EMX 1 2 EN 1 2 FHL 1 2 3 HESX1 HHEX HLX Homeobox A1 A2 A3 A4 A5 A7 A9 A10 A11 A13 B1 B2 B3 B4 B5 B6 B7 B8 B9 B13 C4 C5 C6 C8 C9 C10 C11 C12 C13 D1 D3 D4 D8 D9 D10 D11 D12 D13 HOPX IRX 1 2 3 4 5 6 MKX LMX 1A 1B MEIS 1 2 MEOX2 MNX1 MSX 1 2 NANOG NKX 2-1 2-2 2-3 2-5 3-1 3-2 6-1 6-2 NOBOX PBX 1 2 3 PHF 1 3 6 8 10 16 17 20 21A PHOX 2A 2B PITX 1 2 3 POU domain PIT-1 BRN-3: A B C Octamer transcription factor: 1 2 3/4 6 7 11 OTX 1 2 PDX1 SATB2 SHOX2 SIX 1 2 3 4 5 VAX1 ZEB 1 2

(3.2) Paired box	PAX 1 2 3 4 5 6 7 8 9 PRRX 1 2 RAX

(3.3) Fork head / winged helix	E2F 1 2 3 4 5 FOX proteins A1 A2 A3 C1 C2 D3 D4 E1 E3 F1 G1 H1 I1 J1 J2 K1 K2 L2 M1 N1 N3 O1 O3 O4 P1 P2 P3 P4

(3.4) Heat shock factors	HSF 1 2 4

(3.5) Tryptophan clusters	ELF 2 4 5 EGF ELK 1 3 4 ERF ETS 1 2 ERG SPIB ETV 1 4 5 6 FLI1 Interferon regulatory factors 1 2 3 4 5 6 7 8 MYB MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1 2 3 4

(4) β-Scaffold factors with minor groove contacts

(4.1) Rel homology region	NF-κB NFKB1 NFKB2 REL RELA RELB NFAT C1 C2 C3 C4 5

(4.2) STAT	STAT 1 2 3 4 5 6

(4.3) p53	p53 TBX 1 2 3 5 19 21 22 TBR1 TBR2 TFT MYRF TP63

(4.4) MADS box	Mef2 A B C D SRF

(4.6) TATA-binding proteins	TBP TBPL1

(4.7) High-mobility group	BBX HMGB 1 2 3 4 HMGN 1 2 3 4 HNF 1A 1B LEF1 SOX 1 2 3 4 5 6 8 9 10 11 12 13 14 15 18 21 SRY SSRP1 TCF 3 4 TOX 1 2 3 4

(4.9) Grainyhead	TFCP2

(4.10) Cold-shock domain	CSDA YBX1

(4.11) Runt	CBF CBFA2T2 CBFA2T3 RUNX1 RUNX2 RUNX3 RUNX1T1

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA 1 2 HBP1

(0.3) Pocket domain	Rb RBL1 RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 EREBP B3

(0.6) Miscellaneous	ARID 1A 1B 2 3A 3B 4A CAP IFI 16 35 MLL 2 3 T1 MNDA NFY A B C Rho/Sigma

see also transcription factor/coregulator deficiencies

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TEAD1

Function

Interactions

References

Further reading